| IED ID | IndEnz0002006910 |
| Enzyme Type ID | protease006910 |
| Protein Name |
CAAX prenyl protease 2 EC 3.4.-.- Farnesylated proteins-converting enzyme 2 FACE-2 Prenyl protein-specific endoprotease 2 RCE1 homolog |
| Gene Name | Rce1 Face2 Rce1a |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MAALGGDGLRLLSVSRPERQPESAALSGPGSGLCCWVSVFSCFSLACSYVGSLYVWKSELPRDHPAVIKRRSTSVLVVSSLSPLCVLLWRELTGIQPGTSLLTLMGFRLEGIFPAALLPLLLTMILFLGPLMQLSMDCPCDLTDGLKVVLAPRSWARCLTDMRWLRNQVIAPLTEELVFRACMLPMLAPCTGLGPAVFTCPLFFGVAHFHHIIEQLRFRQSSVGSIFVSAAFQFSYTAVFGAYTAFLFIRTGHLIGPVLCHSFCNYMGFPAVCAALEHPQKWPLLAGYALGVGLFLLLLQPLTDPKLYGSLPLCMLLERTGASETLLCS |
| Enzyme Length | 329 |
| Uniprot Accession Number | P57791 |
| Absorption | |
| Active Site | ACT_SITE 175; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q6LZY8; ACT_SITE 208; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q6LZY8 |
| Activity Regulation | ACTIVITY REGULATION: Deubiquitination by USP17L2/USP17 negatively regulates the proteolytic activity toward Ras GTPases. {ECO:0000250|UniProtKB:Q9Y256}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins. Seems to be able to process K-Ras, N-Ras, H-Ras, RAP1B and G-gamma-1 (By similarity). {ECO:0000250|UniProtKB:Q9Y256, ECO:0000305|PubMed:10085069}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Initiator methionine (1); Modified residue (1); Sequence conflict (2); Site (2); Transmembrane (7) |
| Keywords | Acetylation;Endoplasmic reticulum;Hydrolase;Membrane;Protease;Reference proteome;Transmembrane;Transmembrane helix;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y256}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y256}. |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:Q9Y256 |
| Post Translational Modification | PTM: Ubiquitinated. Undergoes 'Lys-48'- and 'Lys-63'-linked ubiquitination. 'Lys-48' ubiquitination induces its degradation. Deubiquitinated by USP17L2/USP17 that cleaves 'Lys-63'-linked ubiquitin chains (By similarity). {ECO:0000250|UniProtKB:Q9Y256}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10725249; 11217851; 11739732; 12235369; 12433685; 12466851; 14625273; 15659645; 16495543; 16602821; 16973961; 19188362; 21267068; 21555557; 24134311; 32290105; 32398789; 32910507; 9593748; |
| Motif | |
| Gene Encoded By | |
| Mass | 35,867 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.99.B1; |